Esta buscando: Cerium+iron+oxide

Numero del catalogo: (BOSSBS-13591R-A555)

Proveedor: Bioss

Descripción: Proteins internalized into the endocytic pathway are usually degraded. Efficient proteolysis requires denaturation, induced by acidic conditions within lysosomes, and reduction of inter- and intrachain disulfide bonds. Cytosolic reduction is mediated enzymatically by thioredoxin. In the endocytic pathway, reduction of protein disulfide bonds is important for the generation of MHC class II-peptide complexes. This process is catalyzed by a gamma-interferon-inducible thiol reductase (GILT). GILT is synthesized as a precursor, and following delivery to MHC class II-containing compartments (MIICs), is processed to the mature form via cleavage of amino- and carboxy-terminal propeptides. A lysosomal thiol reductase, GILT, is optimally active at low pH and capable of catalyzing disulfide bond reduction both in vivo and in vitro. GILT is expressed constitutively in antigen-presenting cells and is induced by g-interferon in other cell types, suggesting a potentially important role in antigen processing. Additionally, T cell recognition of select exogenous and endogenous epitopes is dependent on tumor cell expression of GILT. The absence of GILT in melanomas alters antigen processing and the hierarchy of immunodominant epitope presentation.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-13591R-FITC)

Proveedor: Bioss

Descripción: Proteins internalized into the endocytic pathway are usually degraded. Efficient proteolysis requires denaturation, induced by acidic conditions within lysosomes, and reduction of inter- and intrachain disulfide bonds. Cytosolic reduction is mediated enzymatically by thioredoxin. In the endocytic pathway, reduction of protein disulfide bonds is important for the generation of MHC class II-peptide complexes. This process is catalyzed by a gamma-interferon-inducible thiol reductase (GILT). GILT is synthesized as a precursor, and following delivery to MHC class II-containing compartments (MIICs), is processed to the mature form via cleavage of amino- and carboxy-terminal propeptides. A lysosomal thiol reductase, GILT, is optimally active at low pH and capable of catalyzing disulfide bond reduction both in vivo and in vitro. GILT is expressed constitutively in antigen-presenting cells and is induced by g-interferon in other cell types, suggesting a potentially important role in antigen processing. Additionally, T cell recognition of select exogenous and endogenous epitopes is dependent on tumor cell expression of GILT. The absence of GILT in melanomas alters antigen processing and the hierarchy of immunodominant epitope presentation.

UOM: 1 * 100 µl

Promoción

Proveedor: Thermo Fisher Scientific

Descripción: Ácido 5-sulfosalicílico dihidrato 99+%

FDS

Numero del catalogo: (PRSI7325P)

Proveedor: ProSci Inc.

Descripción: 16 amino acid peptide near the carboxy terminus of human CRTC2.

UOM: 1 * 50 µG

Promoción

Proveedor: Thermo Fisher Scientific

Descripción: Ácido 5-sulfosalicílico dihidrato ≥98%

FDS Certificados

Numero del catalogo: (PRSI7433P)

Proveedor: ProSci Inc.

Descripción: 19 amino acids near the carboxy terminus of Heartland Virus Glycoprotein 1.

UOM: 1 * 50 µG

Promoción

Proveedor: Thermo Fisher Scientific

Descripción: The carboxy-PEG_n-amine (CA[PEG]n) PEGylation reagents are zwitterionic, amino acid derivatives that are used for modifying proteins or surfaces such as beads, nanoparticles and self-assembled monolayers. These PEGylation reagents are homogenous compounds of defined molecular weight and spacer length, providing precision in optimising modification applications.

Proveedor: Thermo Fisher Scientific

Descripción: Ácido 5-sulfosalicílico dihidrato ACS

FDS

Numero del catalogo: (786-13)

Proveedor: G-Biosciences

Descripción: SG-Chymotrypsin™ is a serine endopeptidase, which predominantly cleaves peptide bonds on the carboxy side of tyrosine, phenylalanine and tryptophan. In addition, chymotrypsin has a low catalytic activity against the carboxy side of leucine, methionine, alanine, aspartic and glutamic acids. It is therefore recommended to always use the shortest digestion time possible.

UOM: 1 * 2 UN

Promoción

Proveedor: Thermo Fisher Scientific

Descripción: Ácido 5-sulfosalicílico dihidrato 99+% ACS

FDS Certificados

Proveedor: Thermo Fisher Scientific

Descripción: Ácido 5-sulfosalicílico dihidrato 98%

FDS

Numero del catalogo: (72687-25G)

Proveedor: Honeywell Chemicals

Descripción: Chromeazurol S (Mordant blue 29) indicator for metal titration, Fluka™

UOM: 1 * 25 g

Promoción

Proveedor: Thermo Fisher Scientific

Descripción: Hidrogenotartrato de colina ≥98%

FDS Certificados

Numero del catalogo: (BOSSBS-13591R-A647)

Proveedor: Bioss

Descripción: Proteins internalized into the endocytic pathway are usually degraded. Efficient proteolysis requires denaturation, induced by acidic conditions within lysosomes, and reduction of inter- and intrachain disulfide bonds. Cytosolic reduction is mediated enzymatically by thioredoxin. In the endocytic pathway, reduction of protein disulfide bonds is important for the generation of MHC class II-peptide complexes. This process is catalyzed by a gamma-interferon-inducible thiol reductase (GILT). GILT is synthesized as a precursor, and following delivery to MHC class II-containing compartments (MIICs), is processed to the mature form via cleavage of amino- and carboxy-terminal propeptides. A lysosomal thiol reductase, GILT, is optimally active at low pH and capable of catalyzing disulfide bond reduction both in vivo and in vitro. GILT is expressed constitutively in antigen-presenting cells and is induced by g-interferon in other cell types, suggesting a potentially important role in antigen processing. Additionally, T cell recognition of select exogenous and endogenous epitopes is dependent on tumor cell expression of GILT. The absence of GILT in melanomas alters antigen processing and the hierarchy of immunodominant epitope presentation.

UOM: 1 * 100 µl

Promoción

Proveedor: MP Biomedicals

Descripción: Desmosine is prepared according to the method of Starcher et al. from hydrolysed neck ligament by solvent extraction and chromatography on Dowex 50.

Numero del catalogo: (BOSSBS-13591R-A750)

Proveedor: Bioss

Descripción: Proteins internalized into the endocytic pathway are usually degraded. Efficient proteolysis requires denaturation, induced by acidic conditions within lysosomes, and reduction of inter- and intrachain disulfide bonds. Cytosolic reduction is mediated enzymatically by thioredoxin. In the endocytic pathway, reduction of protein disulfide bonds is important for the generation of MHC class II-peptide complexes. This process is catalysed by a gamma-interferon-inducible thiol reductase (GILT). GILT is synthesized as a precursor, and following delivery to MHC class II-containing compartments (MIICs), is processed to the mature form via cleavage of amino- and carboxy-terminal propeptides. A lysosomal thiol reductase, GILT, is optimally active at low pH and capable of catalyzing disulfide bond reduction both in vivo and in vitro. GILT is expressed constitutively in antigen-presenting cells and is induced by g-interferon in other cell types, suggesting a potentially important role in antigen processing. Additionally, T cell recognition of select exogenous and endogenous epitopes is dependent on tumor cell expression of GILT. The absence of GILT in melanomas alters antigen processing and the hierarchy of immunodominant epitope presentation.

UOM: 1 * 100 µl

Promoción